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2CA0

Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
A0055114biological_processobsolete oxidation-reduction process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0033068biological_processmacrolide biosynthetic process
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 1407
ChainResidue
ALEU93
APRO289
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
AHIS352
APHE353
ACYS354
AHIS100
AALA360
AARG104
AILE239
ALEU240
AALA243
AGLY244
ATHR247
ATHR248

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PXI A 1408
ChainResidue
AGLU85
ALEU88
AASN89
AGLU94
APHE178
AHIS238
AALA243
AGLU246
ATHR247
AVAL290
AASN392
AMET394
AILE395
AHOH2032

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 1407
ChainResidue
BMET92
BLEU93
BHIS100
BARG104
BPHE111
BALA243
BGLY244
BTHR247
BTHR248
BALA293
BTHR294
BARG296
BALA346
BPHE347
BGLY348
BILE351
BHIS352
BCYS354
BPXI1408

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PXI B 1408
ChainResidue
BTRP74
BGLU85
BLEU93
BGLU94
BPHE178
BHIS238
BVAL242
BALA243
BGLU246
BVAL290
BTHR294
BASN392
BILE395
BHEM1407

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG
ChainResidueDetails
APHE347-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19833867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24627965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2C6H","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2C7X","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CA0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CD8","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZ7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZM","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WHW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WI9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3ZK5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7D","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7S","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4BF4","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU246
ATHR247

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU246
BTHR247

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PDB entries from 2026-09-30

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